Functional Groups and Their Characteristics

  • Hydroxyl:

    • Polar, forms hydrogen bonds.
    • Present in: sugars, some amino acids, alcohols.
  • Carbonyl:

    • Polar.
    • Present in: sugars.
  • Carboxyl:

    • Polar, acidic.
    • Present in: fatty acids, amino acids.
  • Amino:

    • Polar, basic.
    • Forms hydrogen bonds.
    • Present in: amino acids.
  • Sulfhydryl:

    • Polar.
    • Forms disulfide bonds.
    • Present in: some amino acids.
  • Phosphate:

    • Polar, acidic.
    • Present in: nucleotides, phospholipids.

Isomers

  • Definition: Organic molecules with the same molecular formula but different atom arrangements.
    • Example: Butane vs. Isobutane (C4H10).

Monomers, Polymers, and Macromolecules

  • Monomer:

    • Simple molecules; building blocks of polymers.
    • Examples: monosaccharides, amino acids, nucleotides.
  • Polymer:

    • Large molecules formed from many monomers.
    • Examples: polysaccharides, proteins, nucleic acids.
  • Macromolecule:

    • Large biological molecules (proteins, polysaccharides, nucleic acids).

Hydrolysis and Condensation Reactions

  • Condensation/Dehydration synthesis:

    • Monomers link by removing water (hydroxyl and hydrogen).
    • Water is released when bonds are formed.
  • Hydrolysis:

    • Water is added to break down polymers into monomers.
    • Hydroxyl group adds to one monomer and hydrogen to another.

Carbohydrates

Types of glucose
  • Alpha and beta glucose:
    • Isomers differing by the position of the hydroxyl (OH) group on carbon 1.
    • Alpha (α): OH below the ring.
    • Beta (β): OH above the ring.
Energy Storage
  • Starch:

    • Short-term energy storage in plants (found in chloroplasts).
    • Contains amylose (unbranched, α 1,4 bonds) and amylopectin (branched, α 1,4 and α 1,6 bonds).
  • Glycogen:

    • Short-term energy storage in liver/muscles (more branched than amylopectin).
    • Branching via α 1,6 glycosidic bonds.
Structural Polysaccharides
  • Cellulose:

    • Polymer of beta glucose, forms β 1,4 glycosidic bonds.
    • Hydrogen bonds create microfibrils, providing structural support in plants.
  • Chitin:

    • Similar to cellulose with amino groups, found in fungi cell walls and arthropod exoskeletons.

Lipids

Types of Lipids
  • Triglycerides:

    • Composed of glycerol and three fatty acids (ester bonds).
    • Fats (saturated) are solid, oils (unsaturated) are liquid at room temp.
  • Phospholipids:

    • Two fatty acids and a phosphate group, main component of cell membranes.
  • Steroids:

    • Includes cholesterol and hormones (e.g., estrogen, testosterone).
  • Waxes:

    • Prevent water loss, found in plant cuticles.
Fatty Acid Types
  • Saturated fatty acids: No double bonds, solid at room temperature.
  • Unsaturated fatty acids: At least one double bond, liquid at room temperature.

Proteins

  • Polymers of amino acids:

    • Each amino acid has an amino group, carboxyl group, and an R group (determines properties).
  • Levels of protein structure:

    1. Primary Structure: Linear sequence of amino acids (determined by genes).
    2. Secondary Structure: Folding into alpha helices and beta sheets (hydrogen bonds).
    3. Tertiary Structure: 3D shape (bonds: covalent, ionic, hydrogen, hydrophobic interactions, disulfide bonds).
    4. Quaternary Structure: Multiple polypeptide chains (e.g., hemoglobin).
  • Denaturation: Loss of 3D shape due to extreme conditions (pH, temperature).

Nucleic Acids

  • Polymers of nucleotides:

    • Each nucleotide has a nitrogenous base, a pentose sugar, and a phosphate group.
    • Purines: Adenine (A), Guanine (G). Pyrimidines: Cytosine (C), Thymine (T), Uracil (U).
  • DNA vs. RNA:

    • DNA: double-stranded, deoxyribose, base pairing A-T, C-G.
    • RNA: single-stranded, ribose, base pairing A-U, C-G.
  • ATP:

    • Energy currency of the cell, comprises adenine, ribose, and three phosphate groups.
    • ATP hydrolysis releases energy from bonds between phosphates.
Additional Concepts
  • Importance of gene mutations on protein structure and function.
  • Stability variations in proteins affected by R-group interactions.